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Conserved domains on  [gi|1754446051|gb|KAB0407656|]
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hypothetical protein E2I00_019591 [Balaenoptera physalus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
beta-trefoil_Ricin-like super family cl49609
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2777-2884 2.39e-66

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


The actual alignment was detected with superfamily member cd23463:

Pssm-ID: 483949  Cd Length: 136  Bit Score: 221.16  E-value: 2.39e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2777 QPAVYIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSKASDTCLDVIGGRDIPGAKVALWTEHG 2856
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100
                   ....*....|....*....|....*...
gi 1754446051 2857 QFRQKWRLNKNGTISSYLSDQLVLDVKG 2884
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKG 108
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2525-2607 6.88e-29

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 111.82  E-value: 6.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2525 SITLFESDLESGKFIDITnQEISDLEEMGFGSETRSIHVKSGVWVAYQQKFFCGEQYILEKGKYKCFFDWGGSNNIIMSI 2604
Cdd:pfam00030    1 KIVLYEKENFQGRSIELT-DDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSL 79


                   ...
gi 1754446051 2605 RPI 2607
Cdd:pfam00030   80 RPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2613-2687 8.18e-24

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 97.18  E-value: 8.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1754446051 2613 FSKPGFQGECRDFTKEISDLTSSFTP---CSFKVLRGCWLLYYQEDISNHQCVLEEGLYADLTSCGCPTSRVKSLKPI 2687
Cdd:pfam00030    5 YEKENFQGRSIELTDDCPSLQERGFNsrvNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2695-2775 1.85e-21

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


:

Pssm-ID: 459639  Cd Length: 82  Bit Score: 90.63  E-value: 1.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2695 SISLFALEHCEGRELHLEEAVNSVLNKDLHFYTQSVWVKSGLWIAYEGPNFLGRQILLKPNEIPNWTAFSG-WKTIGSLR 2773
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLR 80


                   ..
gi 1754446051 2774 PM 2775
Cdd:pfam00030   81 PI 82
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2295-2381 6.61e-12

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


The actual alignment was detected with superfamily member pfam00030:

Pssm-ID: 470604  Cd Length: 82  Bit Score: 63.28  E-value: 6.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2295 KMVIY---DLHGSKCkqEIYCNIPDATSWSFPNGVL-IKVVRGCWILYEKPHFQGQKCVLEEGEKVLNRDWILQNRKhpq 2370
Cdd:pfam00030    1 KIVLYekeNFQGRSI--ELTDDCPSLQERGFNSRVNsIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDR--- 75

                           90
                   ....*....|.
gi 1754446051 2371 rnfvLGSIKRV 2381
Cdd:pfam00030   76 ----IGSLRPI 82
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 25-49 2.19e-10

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd04157:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 162  Bit Score: 61.68  E-value: 2.19e-10
                           10        20
                   ....*....|....*....|....*
gi 1754446051   25 TFSLSFTVFDMSGQGRYRNLWEHYY 49
Cdd:cd04157     42 KGNLSFTAFDMSGQGKYRGLWEHYY 66
Crystall super family cl02528
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2478-2515 9.46e-06

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


The actual alignment was detected with superfamily member pfam00030:

Pssm-ID: 470604  Cd Length: 82  Bit Score: 45.95  E-value: 9.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1754446051 2478 WVAYEKEHFKGQQFLLEEGDFEDSSACGASSGSILSFR 2515
Cdd:pfam00030   43 WVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLR 80
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 2777-2884 2.39e-66

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467341  Cd Length: 136  Bit Score: 221.16  E-value: 2.39e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2777 QPAVYIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSKASDTCLDVIGGRDIPGAKVALWTEHG 2856
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100
                   ....*....|....*....|....*...
gi 1754446051 2857 QFRQKWRLNKNGTISSYLSDQLVLDVKG 2884
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKG 108
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2525-2607 6.88e-29

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 111.82  E-value: 6.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2525 SITLFESDLESGKFIDITnQEISDLEEMGFGSETRSIHVKSGVWVAYQQKFFCGEQYILEKGKYKCFFDWGGSNNIIMSI 2604
Cdd:pfam00030    1 KIVLYEKENFQGRSIELT-DDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSL 79


                   ...
gi 1754446051 2605 RPI 2607
Cdd:pfam00030   80 RPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2613-2687 8.18e-24

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 97.18  E-value: 8.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1754446051 2613 FSKPGFQGECRDFTKEISDLTSSFTP---CSFKVLRGCWLLYYQEDISNHQCVLEEGLYADLTSCGCPTSRVKSLKPI 2687
Cdd:pfam00030    5 YEKENFQGRSIELTDDCPSLQERGFNsrvNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2526-2607 8.48e-22

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 91.42  E-value: 8.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2526 ITLFESDLESGKFIDITNqEISDLEEMGFGSETRSIHVKSGVWVAYQQKFFCGEQYILEKGKYKCFFDWGGSNNIIMSIR 2605
Cdd:smart00247    2 ITLYEDENFQGRSYELSD-DCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80


                    ..
gi 1754446051  2606 PI 2607
Cdd:smart00247   81 RI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2695-2775 1.85e-21

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 90.63  E-value: 1.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2695 SISLFALEHCEGRELHLEEAVNSVLNKDLHFYTQSVWVKSGLWIAYEGPNFLGRQILLKPNEIPNWTAFSG-WKTIGSLR 2773
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLR 80


                   ..
gi 1754446051 2774 PM 2775
Cdd:pfam00030   81 PI 82
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2781-2892 7.17e-15

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 73.33  E-value: 7.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNvaDTRATSVCISPYSG-KNTQIW-HYCRGLFKSKASDTCLDVigGRDIPGAKVALWTEH-GQ 2857
Cdd:pfam00652    2 TGRIRNRASGKCLDVPGG--SSAGGPVGLYPCHGsNGNQLWtLTGDGTIRSVASDLCLDV--GSTADGAKVVLWPCHpGN 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1754446051 2858 FRQKWRLNKNGT-ISSYLSDqLVLDVKGRPVMKPSV 2892
Cdd:pfam00652   78 GNQRWRYDEDGTqIRNPQSG-KCLDVSGAGTSNGKV 112
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2295-2381 6.61e-12

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 63.28  E-value: 6.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2295 KMVIY---DLHGSKCkqEIYCNIPDATSWSFPNGVL-IKVVRGCWILYEKPHFQGQKCVLEEGEKVLNRDWILQNRKhpq 2370
Cdd:pfam00030    1 KIVLYekeNFQGRSI--ELTDDCPSLQERGFNSRVNsIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDR--- 75

                           90
                   ....*....|.
gi 1754446051 2371 rnfvLGSIKRV 2381
Cdd:pfam00030   76 ----IGSLRPI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2613-2687 1.22e-11

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 62.53  E-value: 1.22e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1754446051  2613 FSKPGFQGECRDFTKEISDLTSSFTPC---SFKVLRGCWLLYYQEDISNHQCVLEEGLYADLTSCGCPTSRVKSLKPI 2687
Cdd:smart00247    5 YEDENFQGRSYELSDDCPSLQDYGSRDnvsSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIRRI 82
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 25-49 2.19e-10

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 61.68  E-value: 2.19e-10
                           10        20
                   ....*....|....*....|....*
gi 1754446051   25 TFSLSFTVFDMSGQGRYRNLWEHYY 49
Cdd:cd04157     42 KGNLSFTAFDMSGQGKYRGLWEHYY 66
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2295-2381 7.02e-10

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 57.52  E-value: 7.02e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2295 KMVIYDLHGSKCKQ-EI---YCNIPDATSWSfpNGVLIKVVRGCWILYEKPHFQGQKCVLEEGEKVLNRDWILQNRKhpq 2370
Cdd:smart00247    1 KITLYEDENFQGRSyELsddCPSLQDYGSRD--NVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQ--- 75

                            90
                    ....*....|.
gi 1754446051  2371 rnfvLGSIKRV 2381
Cdd:smart00247   76 ----ISSIRRI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2727-2775 2.50e-08

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 53.28  E-value: 2.50e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2727 TQSVWVKSGLWIAYEGPNFLGRQILLKPNEIPNWTAFSGWK-TIGSLRPM 2775
Cdd:smart00247   33 VSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNdQISSIRRI 82
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2804-2884 1.60e-07

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 52.13  E-value: 1.60e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2804 ATSVCISPYSGKNT------------QIWHY-CRGLFKSKASDTCLDVIGGRDIPgakVALWTEHGQF-RQKWRLNKNGT 2869
Cdd:smart00458    5 NTGKCLDVNGNKNPvglfdchgtggnQLWKLtSDGAIRIKDTDLCLTANGNTGST---VTLYSCDGTNdNQYWEVNKDGT 81

                            90
                    ....*....|....*
gi 1754446051  2870 ISSYLSDqLVLDVKG 2884
Cdd:smart00458   82 IRNPDSG-KCLDVKD 95
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2478-2515 9.46e-06

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 45.95  E-value: 9.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1754446051 2478 WVAYEKEHFKGQQFLLEEGDFEDSSACGASSGSILSFR 2515
Cdd:pfam00030   43 WVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLR 80
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2830-2888 8.83e-04

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 43.62  E-value: 8.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1754446051 2830 KASDTCLDVIGGRDIPGAKVALWTEHGQFRQKWRlNKNGTISSYLSDQlVLDVK------GRPVM 2888
Cdd:NF035930   164 RVGDLCLDVADGNTRDGARVIAWSCSGGPNQRWR-WRGGQIRSRLSGK-CLDIEggrarpGQPVI 226
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2813-2862 1.27e-03

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 43.24  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2813 SGKNTQIWHYCRGLFKSKASDTCLDVIGGRDIPGAKVALWTEHGQFRQKW 2862
Cdd:NF035930   189 SGGPNQRWRWRGGQIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2478-2515 1.93e-03

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 39.41  E-value: 1.93e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1754446051  2478 WVAYEKEHFKGQQFLLEEGDFEDSSACGASSGSILSFR 2515
Cdd:smart00247   43 WVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 22-123 9.02e-03

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 39.83  E-value: 9.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051   22 VEFTfSLSFTVFDMSGQGRYRNLWEHYYNVENEPM----STSQKKENVLSSEAVKIPQSEDRRNHAekLITLPTQEDskK 97
Cdd:PTZ00133    56 VEYK-NLKFTMWDVGGQDKLRPLWRHYYQNTNGLIfvvdSNDRERIGDAREELERMLSEDELRDAV--LLVFANKQD--L 130

                           90       100
                   ....*....|....*....|....*.
gi 1754446051   98 PNDLSGSTSDAKMGESDKQPKESFFQ 123
Cdd:PTZ00133   131 PNAMSTTEVTEKLGLHSVRQRNWYIQ 156
 
Name Accession Description Interval E-value
beta-trefoil_Ricin_vlAKAP cd23463
ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein ...
 2777-2884 2.39e-66

ricin B-type lectin domain, beta-trefoil fold, found in very large A-kinase anchor protein (vlAKAP) and similar proteins; vlAKAP, also called beta/gamma crystallin domain-containing protein 3 (CRYBG3), is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). vlAKAP belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467341  Cd Length: 136  Bit Score: 221.16  E-value: 2.39e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2777 QPAVYIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSKASDTCLDVIGGRDIPGAKVALWTEHG 2856
Cdd:cd23463      1 QPRVYLRIKNRAQGLYLTTEGNLADPRATSVCVSQYNGKDTQIWYYCRGLLKSKANDACLDVIGGKDNPGSKVALWTEHG 80

                           90       100
                   ....*....|....*....|....*...
gi 1754446051 2857 QFRQKWRLNKNGTISSYLSDQLVLDVKG 2884
Cdd:cd23463     81 KTHQKWRINEDGTISSHLSDDLVLDLKG 108
beta-trefoil_Ricin_CRYBG cd23430
ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin ...
 2780-2884 9.95e-56

ricin B-type lectin domain, beta-trefoil fold, found in the beta/gamma crystallin domain-containing protein (CRYBG) family; The CRYBG family includes three members: CRYBG1, CRYBG2, and CRYBG3/vlAKAP. CRYBG1, also called absent in melanoma 1 protein (AIM1), may function as a suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. CRYBG2 is also called absent in melanoma 1-like protein (AIM1L). CRYBG3/vlAKAP, also called very large A-kinase anchor protein, is an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA). It binds to the dimeric RII-alpha regulatory subunit of PKA (PRKAR2A/PRKAR2B). CRYBG proteins belong to the beta/gamma-crystallin family. They all contain a ricin B-type lectin domain with a beta-trefoil fold at the C-terminus. The beta-trefoil fold is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467308 [Multi-domain]  Cd Length: 133  Bit Score: 190.49  E-value: 9.95e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2780 VYIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSK-ASDTCLDVIGGRDIPGAKVALWTEHGQF 2858
Cdd:cd23430      1 VYFRLRNKATGLFLSVNGNLEDLKLLRVQVMPDVGADDQIWYYQEGLIKCRiAEDCCLTVIGSLVTPGSKVGLWLEQNAD 80

                           90       100
                   ....*....|....*....|....*.
gi 1754446051 2859 RQKWRLNKNGTISSYLSDQLVLDVKG 2884
Cdd:cd23430     81 RQFWSLKSDGRIYSKLKPNLVLDVKG 106
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2525-2607 6.88e-29

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 111.82  E-value: 6.88e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2525 SITLFESDLESGKFIDITnQEISDLEEMGFGSETRSIHVKSGVWVAYQQKFFCGEQYILEKGKYKCFFDWGGSNNIIMSI 2604
Cdd:pfam00030    1 KIVLYEKENFQGRSIELT-DDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSL 79


                   ...
gi 1754446051 2605 RPI 2607
Cdd:pfam00030   80 RPI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2613-2687 8.18e-24

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 97.18  E-value: 8.18e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1754446051 2613 FSKPGFQGECRDFTKEISDLTSSFTP---CSFKVLRGCWLLYYQEDISNHQCVLEEGLYADLTSCGCPTSRVKSLKPI 2687
Cdd:pfam00030    5 YEKENFQGRSIELTDDCPSLQERGFNsrvNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLRPI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2526-2607 8.48e-22

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 91.42  E-value: 8.48e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2526 ITLFESDLESGKFIDITNqEISDLEEMGFGSETRSIHVKSGVWVAYQQKFFCGEQYILEKGKYKCFFDWGGSNNIIMSIR 2605
Cdd:smart00247    2 ITLYEDENFQGRSYELSD-DCPSLQDYGSRDNVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80


                    ..
gi 1754446051  2606 PI 2607
Cdd:smart00247   81 RI 82
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2695-2775 1.85e-21

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 90.63  E-value: 1.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2695 SISLFALEHCEGRELHLEEAVNSVLNKDLHFYTQSVWVKSGLWIAYEGPNFLGRQILLKPNEIPNWTAFSG-WKTIGSLR 2773
Cdd:pfam00030    1 KIVLYEKENFQGRSIELTDDCPSLQERGFNSRVNSIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGApNDRIGSLR 80


                   ..
gi 1754446051 2774 PM 2775
Cdd:pfam00030   81 PI 82
beta-trefoil_Ricin_CRYBG2 cd23465
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ...
 2777-2884 1.71e-18

ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin domain-containing protein 2 (CRYBG2) and similar proteins; CRYBG2, also called absent in melanoma 1-like protein (AIM1L), is a beta/gamma-crystallin family protein with a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467343  Cd Length: 136  Bit Score: 84.15  E-value: 1.71e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2777 QPAVYIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSK-ASDTCLDVIGGRDiPGAKVALWTEH 2855
Cdd:cd23465      1 QRRVYFRLRNRELGLYLAVPDGVEDMKAGRVVVTEQQEGMSHVWFYEDGLLKNQmAPTMSLQVIGPPD-NGAKVVLWSET 79

                           90       100
                   ....*....|....*....|....*....
gi 1754446051 2856 GQFRQKWRLNKNGTISSYLSDQLVLDVKG 2884
Cdd:cd23465     80 RQPRQTWSIQPSGHILSQMFEGMILDVKG 108
beta-trefoil_Ricin_CRYBG1 cd23464
ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin ...
 2777-2884 4.88e-16

ricin B-type lectin domain, beta-trefoil fold, found in beta/gamma crystallin domain-containing protein 1 (CRYBG1) and similar proteins; CRYBG1, also called absent in melanoma 1 protein (AIM1), may function as a suppressor of malignant melanoma. It may exert its effects through interactions with the cytoskeleton. CRYBG1 belongs to the beta/gamma-crystallin family. It contains a ricin B-type lectin domain at the C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467342  Cd Length: 137  Bit Score: 77.15  E-value: 4.88e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2777 QPAVYIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSK-ASDTCLDVIGGRDIPGAKVALWTEH 2855
Cdd:cd23464      1 QKRVYFRLRNKETGCFMSTNGNLDDLKLLRIQVLEDTGSDDQIWVYQDGLIRCRmAEDCCLETVGNLVTAGSKLGLSLEQ 80

                           90       100
                   ....*....|....*....|....*....
gi 1754446051 2856 GQFRQKWRLNKNGTISSYLSDQLVLDVKG 2884
Cdd:cd23464     81 GKDNQFWSITSDGRIYSKLKPDLVLDIKG 109
Ricin_B_lectin pfam00652
Ricin-type beta-trefoil lectin domain;
2781-2892 7.17e-15

Ricin-type beta-trefoil lectin domain;


Pssm-ID: 395527 [Multi-domain]  Cd Length: 126  Bit Score: 73.33  E-value: 7.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNvaDTRATSVCISPYSG-KNTQIW-HYCRGLFKSKASDTCLDVigGRDIPGAKVALWTEH-GQ 2857
Cdd:pfam00652    2 TGRIRNRASGKCLDVPGG--SSAGGPVGLYPCHGsNGNQLWtLTGDGTIRSVASDLCLDV--GSTADGAKVVLWPCHpGN 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1754446051 2858 FRQKWRLNKNGT-ISSYLSDqLVLDVKGRPVMKPSV 2892
Cdd:pfam00652   78 GNQRWRYDEDGTqIRNPQSG-KCLDVSGAGTSNGKV 112
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2781-2884 7.67e-15

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 73.56  E-value: 7.67e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNvADTRATSVCISPYSGKNTQIWHY-----CRGLFKSKASDTCLDVIGGRDIPGAKVALWTEH 2855
Cdd:cd00161      2 TYRIVNAASGKCLDVAGG-STANGAPVQQWTCNGGANQQWTLtpvgdGYYTIRNVASGKCLDVAGGSTANGANVQQWTCN 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1754446051 2856 GQFRQKWRLNKNG----TISSYLSDqLVLDVKG 2884
Cdd:cd00161     81 GGDNQQWRLEPVGdgyyRIVNKHSG-KCLDVSG 112
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2295-2381 6.61e-12

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 63.28  E-value: 6.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2295 KMVIY---DLHGSKCkqEIYCNIPDATSWSFPNGVL-IKVVRGCWILYEKPHFQGQKCVLEEGEKVLNRDWILQNRKhpq 2370
Cdd:pfam00030    1 KIVLYekeNFQGRSI--ELTDDCPSLQERGFNSRVNsIRVLSGAWVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDR--- 75

                           90
                   ....*....|.
gi 1754446051 2371 rnfvLGSIKRV 2381
Cdd:pfam00030   76 ----IGSLRPI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2613-2687 1.22e-11

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 62.53  E-value: 1.22e-11
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1754446051  2613 FSKPGFQGECRDFTKEISDLTSSFTPC---SFKVLRGCWLLYYQEDISNHQCVLEEGLYADLTSCGCPTSRVKSLKPI 2687
Cdd:smart00247    5 YEDENFQGRSYELSDDCPSLQDYGSRDnvsSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIRRI 82
beta-trefoil_Ricin-like cd00161
ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a ...
 2781-2862 8.82e-11

ricin B-type lectin domain, beta-trefoil fold; The ricin B-type lectin domain is a carbohydrate-binding domain formed from presumed gene triplication. It shows a beta-trefoil fold characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ricin B-type lectin domain was originally found in Ricin, which is a legume lectin from the seeds of the castor bean plant, Ricinus communis. It is also found in many carbohydrate-recognition proteins like plant and bacterial AB-toxins, glycosidases, or proteases, which serve diverse functions such as inhibitory toxicity, enzymatic activity, and signal transduction. The ricin B-type lectin domain can be present in one or more copies and has been shown in some instances to bind simple sugars, such as galactose or lactose. The most characteristic, though not completely conserved, sequence feature is the presence of a Q-W pattern. Consequently, the ricin B-type lectin domain has also been referred as the (QxW)3 domain and the three homologous regions as the QxW repeats. A disulfide bond is also conserved in some QxW repeats.


Pssm-ID: 467293 [Multi-domain]  Cd Length: 134  Bit Score: 62.00  E-value: 8.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNVADTRATsVCISPYSGKNTQIWHY-----CRGLFKSKASDTCLDVIGGRDIPGAKVALWTEH 2855
Cdd:cd00161     49 YYTIRNVASGKCLDVAGGSTANGAN-VQQWTCNGGDNQQWRLepvgdGYYRIVNKHSGKCLDVSGGSTANGANVQQWTCN 127


                   ....*..
gi 1754446051 2856 GQFRQKW 2862
Cdd:cd00161    128 GGANQQW 134
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2778-2885 1.16e-10

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 61.60  E-value: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2778 PAVYIRIKNRAQDEYLTVTGNVAdTRATSVCISPYSGKNTQIWHYC-RGLFKSKAsDTCLDVIGGRDIPGAKVALWTEHG 2856
Cdd:cd23418      2 GAGGGQIRGYGSGRCLDVPGGST-TNGTRLILWDCHGGANQQFTFTsAGELRVGG-DKCLDAAGGGTTNGTPVVIWPCNG 79

                           90       100
                   ....*....|....*....|....*....
gi 1754446051 2857 QFRQKWRLNKNGTISSYLSDqLVLDVKGR 2885
Cdd:cd23418     80 GANQKWRFNSDGTIRNVNSG-LCLDVAGG 107
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
 25-49 2.19e-10

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 61.68  E-value: 2.19e-10
                           10        20
                   ....*....|....*....|....*
gi 1754446051   25 TFSLSFTVFDMSGQGRYRNLWEHYY 49
Cdd:cd04157     42 KGNLSFTAFDMSGQGKYRGLWEHYY 66
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2295-2381 7.02e-10

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 57.52  E-value: 7.02e-10
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2295 KMVIYDLHGSKCKQ-EI---YCNIPDATSWSfpNGVLIKVVRGCWILYEKPHFQGQKCVLEEGEKVLNRDWILQNRKhpq 2370
Cdd:smart00247    1 KITLYEDENFQGRSyELsddCPSLQDYGSRD--NVSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQ--- 75

                            90
                    ....*....|.
gi 1754446051  2371 rnfvLGSIKRV 2381
Cdd:smart00247   76 ----ISSIRRI 82
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2727-2775 2.50e-08

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 53.28  E-value: 2.50e-08
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2727 TQSVWVKSGLWIAYEGPNFLGRQILLKPNEIPNWTAFSGWK-TIGSLRPM 2775
Cdd:smart00247   33 VSSVRVESGCWVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNdQISSIRRI 82
beta-trefoil_Ricin_GllA-1 cd23454
GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; ...
 2784-2904 3.99e-08

GllA-1 domain, beta-trefoil fold, found in Mucor circinelloides Gellins and similar proteins; Gellin proteins act as central effectors of wound-induced protoplasmic gelation. They possess ten related N-terminal beta-trefoil domains (Gll-1 to Gll-10) that contribute to distinct gelation-related activities. The beta-trefoil domains show low sequence similarity to members of the functionally diverse ricin B lectin domain family. They are characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site. Gellin from M. circinelloides has been called GellinA (also known as GllA). The model corresponds to GllA-1 domain, which is a remote family member of the ricin B-type lectin domain.


Pssm-ID: 467332 [Multi-domain]  Cd Length: 136  Bit Score: 54.63  E-value: 3.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2784 IKNRAQDEYLTV-TGNVADTRATSVCISPYSGKNTQIWHYCRGLFKSKASDTCLDVIGGRDIPGAKVALW---TEHGQFR 2859
Cdd:cd23454      5 IKSSSNGLVLDVeHGSLKSGAKVVLAPLKTKDYESQLWRYDDGYLVNKASGLVLDIQGGVVKSGTRLVQSpkkPSKDANN 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1754446051 2860 QKWRLNKNGTISSYLSDQLVLDVKGRPVMKPSvlcpRIFILNSKP 2904
Cdd:cd23454     85 QRWGLTADGYIYLLSNPSLVLGIKGNETREGA----RVILQERKL 125
beta-trefoil_Ricin_SCDase cd23456
ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide ...
 2781-2884 4.77e-08

ricin B-type lectin domain, beta-trefoil fold, found in Shewanella algae sphingolipid ceramide N-deacylase (SCDase) and similar proteins; SCDase (EC 3.5.1.69) is an enzyme which hydrolyzes the N-acyl linkage between fatty acid and sphingosine in ceramide of various glycosphingolipids and sphingomyelin. Shewanella algae SCDase contains two ricin B-type lectin domains at its C-terminus. The ricin B-type lectin domain shows a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may harbor a sugar-binding pocket.


Pssm-ID: 467334 [Multi-domain]  Cd Length: 122  Bit Score: 53.90  E-value: 4.77e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNVadTRATSVCISPYSGKNTQIWHY-CRGLFKSKA-SDTCLDVIGGRDiPGAKVALWTEHGQF 2858
Cdd:cd23456      2 YFQLKSQASGLCLDVSGGA--TNGANVVVYDCNNSNSQKWYYdATGRLHSKAnPGKCLDAGGENS-NGANVVLWACNDSA 78

                           90       100
                   ....*....|....*....|....*.
gi 1754446051 2859 RQKWRLNkNGTISSYLSDQLVLDVKG 2884
Cdd:cd23456     79 NQRWDFD-GNFIRSRNNTNLALDAYG 103
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2804-2884 1.60e-07

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 52.13  E-value: 1.60e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2804 ATSVCISPYSGKNT------------QIWHY-CRGLFKSKASDTCLDVIGGRDIPgakVALWTEHGQF-RQKWRLNKNGT 2869
Cdd:smart00458    5 NTGKCLDVNGNKNPvglfdchgtggnQLWKLtSDGAIRIKDTDLCLTANGNTGST---VTLYSCDGTNdNQYWEVNKDGT 81

                            90
                    ....*....|....*
gi 1754446051  2870 ISSYLSDqLVLDVKG 2884
Cdd:smart00458   82 IRNPDSG-KCLDVKD 95
beta-trefoil_Ricin_XLN-like cd23418
ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1, ...
 2796-2863 2.40e-07

ricin B-type lectin domain, beta-trefoil fold, found in Streptomyces olivaceoviridis endo-1,4-beta-xylanase and similar proteins; The family includes Streptomyces olivaceoviridis endo-1,4-beta-xylanase (XLN, EC 3.2.1.8), Streptomyces avermitilis beta-L-arabinopyranosidase (EC 3.2.1.185), and Streptomyces coelicolor extracellular exo-alpha-L-arabinofuranosidase (ABF, EC 3.2.1.55). XLN, also called xylanase, or 1,4-beta-D-xylan xylanohydrolase, belongs to the glycosyl hydrolase 10 (cellulase F) family. It contributes to hydrolyze hemicellulose, the major component of plant cell walls. XLN contains a (beta/alpha)8-barrel as a catalytic domain, a family 13 carbohydrate binding module (CBM13) as a xylan binding domain (XBD) and a Gly/Pro-rich linker between them. Beta-L-arabinopyranosidase belongs to the glycosyl hydrolase 27 (GH27) family. It has a GH27 catalytic domain, an antiparallel beta-domain containing Greek key motifs, another antiparallel beta-domain forming a jellyroll structure, and a CBM13 module. ScAraf62A, also called ABF, or arabinosidase, or arabinoxylan arabinofuranohydrolase, belongs to the glycosyl hydrolase 62 (GH62) family. It is involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. It acts synergistically with xylanases and binds specifically to xylan. ScAraf62A comprises a CBM13 module at its N-terminus and a catalytic domain at its C-terminus. This model corresponds to the CBM13 module, which is a ricin B-type lectin domain with a beta-trefoil fold, characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain may contain a potential sugar-binding pocket.


Pssm-ID: 467297 [Multi-domain]  Cd Length: 130  Bit Score: 51.97  E-value: 2.40e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1754446051 2796 TGNVADTRATSVCISPYSGKNTQIWH-YCRGLFKSKASDTCLDVIGGRDIPGAKVALWTEHGQFRQKWR 2863
Cdd:cd23418     61 AAGGGTTNGTPVVIWPCNGGANQKWRfNSDGTIRNVNSGLCLDVAGGGTANGTRLILWSCNGGSNQRWR 129
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
2827-2884 8.94e-07

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 49.30  E-value: 8.94e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1754446051 2827 FKSKASDTCLDVIGGRDIPGAKVALWTEHGQFRQKWRLNKNG----TISSYLSDqLVLDVKG 2884
Cdd:pfam14200   18 IVNVASGKYLDVAGGSTANGANVQQWTDNGNDNQQWRIVDAGdgyyRIVNKASG-KVLDVAG 78
Crystall pfam00030
Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity ...
 2478-2515 9.46e-06

Beta/Gamma crystallin; The alignment comprises two Greek key motifs since the similarity between them is very low.


Pssm-ID: 459639  Cd Length: 82  Bit Score: 45.95  E-value: 9.46e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1754446051 2478 WVAYEKEHFKGQQFLLEEGDFEDSSACGASSGSILSFR 2515
Cdd:pfam00030   43 WVLYEHPNFRGRQYVLEPGEYPDWSDWGAPNDRIGSLR 80
RicinB_lectin_2 pfam14200
Ricin-type beta-trefoil lectin domain-like;
2781-2852 2.55e-05

Ricin-type beta-trefoil lectin domain-like;


Pssm-ID: 464102 [Multi-domain]  Cd Length: 89  Bit Score: 45.06  E-value: 2.55e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNvADTRATSVCISPYSGKNTQIWH-------YCRglFKSKASDTCLDVIGGRDiPGAKVALW 2852
Cdd:pfam14200   15 YYTIVNVASGKYLDVAGG-STANGANVQQWTDNGNDNQQWRivdagdgYYR--IVNKASGKVLDVAGSTA-NGTNVQQW 89
beta-trefoil_Ricin_EW29-like cd23449
ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa ...
 2828-2884 4.14e-05

ricin B-type lectin domain, beta-trefoil fold, found in Lumbricus terrestris 29-kDa galactose-binding lectin (EW29) and similar proteins; EW29 is a galactose-binding lectin from the earthworm Lumbricus terrestris. It contains two ricin B-type lectin domains with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The second ricin B-type lectin domain may harbor two sugar-binding pockets in subdomains alpha and gamma. EW29 uses these two sugar-binding sites for its function as a single domain-type hemagglutinin.


Pssm-ID: 467327 [Multi-domain]  Cd Length: 128  Bit Score: 45.36  E-value: 4.14e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2828 KSKASDTCLDVIGGRDIPGAKVALWTEHG--QFRQKWRLNK-NGTISSYLSDqLVLDVKG 2884
Cdd:cd23449      6 KSKLNGKVLDVEGANAKPGAKVIMWEKKGgaEDNQLWYEDEvTGTIRSKLND-FCLDASG 64
beta-trefoil_Ricin_AgaB34-like cd23458
ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 ...
 2781-2884 6.76e-05

ricin B-type lectin domain, beta-trefoil fold, found in Agarivorans albus beta-agarase AgaB34 and similar proteins; Beta-agarase (EC 3.2.1.81), also called endo-beta-agarase, is a glycosyl hydrolase family 16 (GH16) member that catalyzes the hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose, a hydrophilic polysaccharide found in the cell wall of Rhodophyceaea (marine red algae), giving the tetramer as the predominant product. Beta-agarase contains a ricin B-type lectin domain that adopts a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467336 [Multi-domain]  Cd Length: 135  Bit Score: 45.01  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGNVADTRATSVCISPYSGKNtQIWH-------YCRglFKSKASDTCLDVIGGRDIPGAKVALWT 2853
Cdd:cd23458      2 TYRIRNRNSGKCIDVAGGSTANGANIQQWDCGSGSN-QQWTlveidngYYR--IKASHSGKCLDVAGGSTANGANIQQWD 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1754446051 2854 EHGQFRQKWRLNKNG----TISSYLSDQlVLDVKG 2884
Cdd:cd23458     79 CVGGANQQWKLQDLGngyfELKARHSGK-CLDVAG 112
RICIN smart00458
Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.
 2783-2864 7.44e-05

Ricin-type beta-trefoil; Carbohydrate-binding domain formed from presumed gene triplication.


Pssm-ID: 214672 [Multi-domain]  Cd Length: 118  Bit Score: 44.42  E-value: 7.44e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051  2783 RIKNRAQDEYLTVTGNvadtRATSVCISPYSGKN-TQIWHYCR-GLFKSKASDTCLDVIGGRdiPGAKVALWTEHGQFRQ 2860
Cdd:smart00458   40 AIRIKDTDLCLTANGN----TGSTVTLYSCDGTNdNQYWEVNKdGTIRNPDSGKCLDVKDGN--TGTKVILWTCSGNPNQ 113


                    ....
gi 1754446051  2861 KWRL 2864
Cdd:smart00458  114 KWIF 117
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 28-50 1.31e-04

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 44.87  E-value: 1.31e-04
                           10        20
                   ....*....|....*....|...
gi 1754446051   28 LSFTVFDMSGQGRYRNLWEHYYN 50
Cdd:cd00878     43 VKFTVWDVGGQDKIRPLWKHYYE 65
IL4_i_Ig pfam18258
Interleukin-4 inducing immunoglobulin-binding domain; This domain is found in Interleukin-4 ...
 2728-2772 6.21e-04

Interleukin-4 inducing immunoglobulin-binding domain; This domain is found in Interleukin-4 inducing protein alpha-1 (IPSE/alpha-1) present in Schistosoma mansoni, a parasite of humans. IPSE/alpha-1 triggers the release of IL-4 from basophils in the liver which is a major site of egg deposition during S. mansoni infection. This domain adopts a beta gamma-crystallin fold that is stabilized by three disulfide bonds within the domain (23/26, 59/93, and 111/121). The domain is involved in immunoglobulin binding.


Pssm-ID: 408073  Cd Length: 89  Bit Score: 40.93  E-value: 6.21e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1754446051 2728 QSVWVKSGLWIAYEGPNFLGRQILLKPNE-IPNWTAFsGWKTIGSL 2772
Cdd:pfam18258   40 NQWYKRSTYWLIYEQPHFNGRYLLLKPGEcIDNVRQY-GLLSISSI 84
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2830-2888 8.83e-04

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 43.62  E-value: 8.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1754446051 2830 KASDTCLDVIGGRDIPGAKVALWTEHGQFRQKWRlNKNGTISSYLSDQlVLDVK------GRPVM 2888
Cdd:NF035930   164 RVGDLCLDVADGNTRDGARVIAWSCSGGPNQRWR-WRGGQIRSRLSGK-CLDIEggrarpGQPVI 226
lectin_2 NF035930
lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host ...
 2813-2862 1.27e-03

lectin; Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor.


Pssm-ID: 468267 [Multi-domain]  Cd Length: 238  Bit Score: 43.24  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2813 SGKNTQIWHYCRGLFKSKASDTCLDVIGGRDIPGAKVALWTEHGQFRQKW 2862
Cdd:NF035930   189 SGGPNQRWRWRGGQIRSRLSGKCLDIEGGRARPGQPVIVWSCNGGPNQRW 238
beta-trefoil_Ricin_1,3Gal43A cd23446
ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and ...
 2781-2864 1.64e-03

ricin B-type lectin domain, beta-trefoil fold, found in Clostridium thermocellum 1,3Gal43A and similar proteins; 1,3Gal43A is an exo-beta-1,3-galactanase that specifically hydrolyses beta-1,3 glycosidic bonds in galactose-based oligosaccharides or polysaccharides, and shows maximum activity towards beta-1,3-galactotetraose. 1,3Gal43A consists of a glycoside hydrolase family 43 (GH43) catalytic domain, a CBM13 carbohydrate binding domain, and a type I dockerin domain. The CBM13 domain is also known as the ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467324 [Multi-domain]  Cd Length: 137  Bit Score: 41.21  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2781 YIRIKNRAQDEYLTVTGnvADTRATSVCIS-PYSGKNTQIWHYC---RGLFK--SKASDTCLDVIGGRDIPGAKVALWTE 2854
Cdd:cd23446     49 YYKIVNRNSGKALDVNG--ASTADGAAIIQwTSNGGDNQQWQIVdtgDGYYKivNRNSGKLLDVNGWSTADGADIIQWSD 126

                           90
                   ....*....|
gi 1754446051 2855 HGQFRQKWRL 2864
Cdd:cd23446    127 NGGTNQQWQL 136
beta-trefoil_Ricin_RPI cd23452
ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine ...
 2808-2884 1.91e-03

ricin B-type lectin domain, beta-trefoil fold, found in Rarobacter faecitabidus serine protease I (RPI) and similar proteins; RPI, also called serine protease 1, is a major serine protease exhibiting lytic activity toward living yeast cells. It has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI. RPI contains a C-terminal ricin B-type lectin domain with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. Each subdomain bears a potential sugar binding site.


Pssm-ID: 467330 [Multi-domain]  Cd Length: 125  Bit Score: 40.58  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051 2808 CISPYSGKNT-----QIWHyCRGLFKSK---ASD-------TCLDVIGGRDIPGAKVALWTEHGQFRQKWRLNKNGTISS 2872
Cdd:cd23452     13 CIDVPNSSTTdgaplQLWD-CNGTNAQKwtfASDgtlralgKCLDVAWGGTDNGTAVQLWTCSGNPAQQFVLSGAGDLVN 91

                           90
                   ....*....|..
gi 1754446051 2873 YLSDQLVlDVKG 2884
Cdd:cd23452     92 PQANKCV-DVSG 102
XTALbg smart00247
Beta/gamma crystallins; Beta/gamma crystallins
 2478-2515 1.93e-03

Beta/gamma crystallins; Beta/gamma crystallins


Pssm-ID: 214583  Cd Length: 82  Bit Score: 39.41  E-value: 1.93e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1754446051  2478 WVAYEKEHFKGQQFLLEEGDFEDSSACGASSGSILSFR 2515
Cdd:smart00247   43 WVLYEQPNYRGRQYVLEPGEYPDYQEWGGFNDQISSIR 80
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
 22-123 9.02e-03

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 39.83  E-value: 9.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1754446051   22 VEFTfSLSFTVFDMSGQGRYRNLWEHYYNVENEPM----STSQKKENVLSSEAVKIPQSEDRRNHAekLITLPTQEDskK 97
Cdd:PTZ00133    56 VEYK-NLKFTMWDVGGQDKLRPLWRHYYQNTNGLIfvvdSNDRERIGDAREELERMLSEDELRDAV--LLVFANKQD--L 130

                           90       100
                   ....*....|....*....|....*.
gi 1754446051   98 PNDLSGSTSDAKMGESDKQPKESFFQ 123
Cdd:PTZ00133   131 PNAMSTTEVTEKLGLHSVRQRNWYIQ 156
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
 22-50 9.80e-03

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).


Pssm-ID: 206717 [Multi-domain]  Cd Length: 159  Bit Score: 39.31  E-value: 9.80e-03
                           10        20
                   ....*....|....*....|....*....
gi 1754446051   22 VEFTfSLSFTVFDMSGQGRYRNLWEHYYN 50
Cdd:cd04150     39 VEYK-NISFTVWDVGGQDKIRPLWRHYFQ 66
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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